Backbone assignment of perdeuterated proteins using long-range H/C-dipolar transfers
Backbone assignment of perdeuterated proteins using long-range H/C-dipolar transfers
Abstract For micro-crystalline proteins, solid-state nuclear magnetic resonance spectroscopy of perdeuterated samples can provide spectra of unprecedented quality. Apart from allowing to detect sparsely introduced protons and thereby increasing the effective resolution for a series of sophisticated techniques, deuteration can provide extraordinary coherence lifetimesâ??obtainable for all involved nuclei virtually without decoupling and enabling the use of scalar magnetization transfers. Unfortunately,...
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Structure Calculation from Unambiguous Long-Range Amide and Methyl (1)H-(1)H Distance Restraints for a Microcrystalline Protein with MAS Solid-State NMR Spectroscopy.
Structure Calculation from Unambiguous Long-Range Amide and Methyl (1)H-(1)H Distance Restraints for a Microcrystalline Protein with MAS Solid-State NMR Spectroscopy.
Structure Calculation from Unambiguous Long-Range Amide and Methyl (1)H-(1)H Distance Restraints for a Microcrystalline Protein with MAS Solid-State NMR Spectroscopy.
J Am Chem Soc. 2011 Mar 24;
Authors: Linser R, Bardiaux B, Higman V, Fink U, Reif B
Magic-angle spinning (MAS) solid-state NMR becomes an increasingly important tool for the determination of structures of membrane...
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03-26-2011 07:00 PM
Structure Calculation from Unambiguous Long-Range Amide and Methyl 1H-1H Distance Restraints for a Microcrystalline Protein with MAS Solid-State NMR Spectroscopy
Structure Calculation from Unambiguous Long-Range Amide and Methyl 1H-1H Distance Restraints for a Microcrystalline Protein with MAS Solid-State NMR Spectroscopy
Rasmus Linser, Benjamin Bardiaux, Victoria Higman, Uwe Fink and Bernd Reif
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja110222h/aop/images/medium/ja-2010-10222h_0004.gif
Journal of the American Chemical Society
DOI: 10.1021/ja110222h
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[NMR paper] Characterization of threonine side chain dynamics in an antifreeze protein using natu
Characterization of threonine side chain dynamics in an antifreeze protein using natural abundance 13C NMR spectroscopy.
Related Articles Characterization of threonine side chain dynamics in an antifreeze protein using natural abundance 13C NMR spectroscopy.
J Biomol NMR. 2004 Jun;29(2):139-50
Authors: Daley ME, Sykes BD
The dynamics of threonine side chains of the Tenebrio molitor antifreeze protein (TmAFP) were investigated using natural abundance (13)C NMR. In TmAFP, the array of threonine residues on one face of the protein is responsible...
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11-24-2010 09:51 PM
[NMR paper] Measurement of long-range cross-correlation rates using a combination of single- and
Measurement of long-range cross-correlation rates using a combination of single- and multiple-quantum NMR spectroscopy in one experiment.
Related Articles Measurement of long-range cross-correlation rates using a combination of single- and multiple-quantum NMR spectroscopy in one experiment.
J Am Chem Soc. 2002 Apr 17;124(15):4050-7
Authors: Fruh D, Chiarparin E, Pelupessy P, Bodenhausen G
A method is described to determine long-range cross-correlations between the modulations of an anisotropic chemical shift (e.g., of a C' carbonyl carbon in...
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11-24-2010 08:49 PM
[NMR paper] De novo determination of protein structure by NMR using orientational and long-range
De novo determination of protein structure by NMR using orientational and long-range order restraints.
Related Articles De novo determination of protein structure by NMR using orientational and long-range order restraints.
J Mol Biol. 2000 May 19;298(5):927-36
Authors: Hus JC, Marion D, Blackledge M
Orientational and novel long-range order restraints available from paramagnetic systems have been used to determine the backbone solution structure of the cytochrome c' protein to atomic resolution in the complete absence of restraints derived from...
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11-18-2010 09:15 PM
[NMR paper] Defining long range order in NMR structure determination from the dependence of heter
Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy.
Related Articles Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy.
Nat Struct Biol. 1997 Jun;4(6):443-9
Authors: Tjandra N, Garrett DS, Gronenborn AM, Bax A, Clore GM
Structure determination by NMR presently relies on short range restraints between atoms in close spatial proximity, principally in the...
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08-22-2010 03:31 PM
[NMR paper] Defining long range order in NMR structure determination from the dependence of heter
Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy.
Related Articles Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy.
Nat Struct Biol. 1997 Jun;4(6):443-9
Authors: Tjandra N, Garrett DS, Gronenborn AM, Bax A, Clore GM
Structure determination by NMR presently relies on short range restraints between atoms in close spatial proximity, principally in the...
Antifreeze Glycoprotein Activity Correlates with Long-Range Protein-Water Dynamics
Journal of the American Chemical Society, Volume 0, Issue 0, Articles ASAP (As Soon As Publishable). 
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